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Title:Exploring the Roles of Heme Type and Histidine -Tyrosine Cross -Link in Heme-Copper Oxidases Using a Myoglobin Model
Author(s):Wang, Ningyan
Doctoral Committee Chair(s):Lu, Yi
Department / Program:Biochemistry
Degree Granting Institution:University of Illinois at Urbana-Champaign
Subject(s):Chemistry, Biochemistry
Abstract:Novel oxygen reactivity is observed in our model protein (CuBMb) which reproduces the most essential components of HCO active site. In order to improve this artificial model to inhibit its side reaction with oxygen and channel it toward oxidase reactivity, more features were introduced into the CuBMb model in this study: (1) synthetic heme cofactors are used to replace the natural one of the protein, resulting in ∼20 fold inhibition of the side reaction; (2) a novel semi-synthetic system (Expressed Protein Ligation) is also established that may introduce new features such as the Tyr-His cross-linking structure in HCO to the model by direct incorporation of unnatural amino acid(s) into the protein sequence. These strategies demonstrate the power of combining the strength of biological, chemical and modern analytical techniques to create accurate biosynthesis models of protein active sites which can provide insight not easily achievable through other studies, thereby complementing the knowledge gained from both native protein and synthetic model studies.
Issue Date:2007
Description:129 p.
Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2007.
Other Identifier(s):(MiAaPQ)AAI3290422
Date Available in IDEALS:2015-09-25
Date Deposited:2007

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